Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/171596
Title: Myoglobinopathy is an adult-onset autosomal dominant myopathy with characteristic sarcoplasmic inclusions
Author: Olivé i Plana, Montserrat
Engvall, Martin
Ravenscroft, Gianina
Cabrera Serrano, Macarena
Jiao, Hong
Bortolotti, Carlo Augusto
Pignataro, Marcello
Lambrughi, Matteo
Jiang, Haibo
Forrest, Alistair R. R.
Benseny Cases, Núria
Hofbauer, Stefan
Obinger, Christian
Battistuzzi, Gianantonio
Bellei, Marzia
Borsari, Marco
Di Rocco, Giulia
Viola, Helena M.
Hoo, Livia C.
Cladera, Josep
Lagerstedt Robinson, Kristina
Xiang, Fengqing
Wredenberg, Anna
Miralles, Francesc
Baiges, Juan José
Malfatti, Edoardo
Romero, Norma B.
Streichenberger, Nathalie
Via, Christophe
Claeys, Kristl G.
Straathof, Chiara S.M
Goris, An
Freyer, Christoph
Lammens, Martin
Bassez, Guillaume
Kere, Juha
Clemente, Paula
Sejersen, Thomas
Udd, Bjarne
Vidal, Noemí
Ferrer, Isidro (Ferrer Abizanda)
Edstrom, Lars
Wedell, Anna
Laing, Niger G.
Keywords: Malalties musculars
Mutació (Biologia)
Muscular Diseases
Mutation (Biology)
Issue Date: 1-Jan-2019
Publisher: Nature Publishing Group
Abstract: Myoglobin, encoded by MB, is a small cytoplasmic globular hemoprotein highly expressed in cardiac myocytes and oxidative skeletal myofibers. Myoglobin binds O-2, facilitates its intracellular transport and serves as a controller of nitric oxide and reactive oxygen species. Here, we identify a recurrent c.292C>T ( p.His98Tyr) substitution in MB in fourteen members of six European families suffering from an autosomal dominant progressive myopathy with highly characteristic sarcoplasmic inclusions in skeletal and cardiac muscle. Myoglobinopathy manifests in adulthood with proximal and axial weakness that progresses to involve distal muscles and causes respiratory and cardiac failure. Biochemical characterization reveals that the mutant myoglobin has altered O-2 binding, exhibits a faster heme dissociation rate and has a lower reduction potential compared to wild-type myoglobin. Preliminary studies show that mutant myoglobin may result in elevated superoxide levels at the cellular level. These data define a recognizable muscle disease associated with MB mutation.
Note: Reproducció del document publicat a: https://doi.org/10.1038/s41467-019-09111-2
It is part of: Nature Communications, 2019-01-01, Vol. 10, num. 1396
URI: http://hdl.handle.net/2445/171596
Related resource: https://doi.org/10.1038/s41467-019-09111-2
Appears in Collections:Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL))

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